Actin‐Stimulated Myosin Mg2+‐ATPase Inhibition by Brain Protein

S. Berl; M. Chou; C. Mytilineou

doi:10.1111/j.1471-4159.1983.tb13582.x

Actin‐Stimulated Myosin Mg²⁺‐ATPase Inhibition by Brain Protein

S. Berl
, M. Chou
, C. Mytilineou

Icahn School of Medicine at Mount Sinai

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

Abstract: A low‐molecular‐weight protein, isolated from bovine brain, inhibits the actin‐stimulated Mg‐ATPase activity of myosin from striated muscle. This inhibition is probably related to its ability to cause actin to revert from its polymerized to its depolymerized state and to prevent the polymerization of actin. Its effect on the polymeric state of the actin has been demonstrated by viscosity studies, DNase inhibition assay, and electron microscopy. Heavy meromyosin can overcome the effect of the brain protein and stimulate the polymerization of actin. The inhibition of ATPase activity is in part dependent upon the relative amounts of brain protein, actin, and myosin. The apparent molecular weight of the brain protein is approximately 20,000 daltons. It appears to be a heat‐labile glycoprotein containing 5–6% carbohydrate. 1983 International Society for Neurochemistry

Original language	English
Pages (from-to)	1397-1405
Number of pages	9
Journal	Journal of Neurochemistry
Volume	40
Issue number	5
DOIs	https://doi.org/10.1111/j.1471-4159.1983.tb13582.x
State	Published - May 1983

Keywords

Actin activation
Brain inhibitory protein
Myosin ATPase

Access to Document

10.1111/j.1471-4159.1983.tb13582.x

Cite this

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title = "Actin‐Stimulated Myosin Mg2+‐ATPase Inhibition by Brain Protein",

abstract = "Abstract: A low‐molecular‐weight protein, isolated from bovine brain, inhibits the actin‐stimulated Mg‐ATPase activity of myosin from striated muscle. This inhibition is probably related to its ability to cause actin to revert from its polymerized to its depolymerized state and to prevent the polymerization of actin. Its effect on the polymeric state of the actin has been demonstrated by viscosity studies, DNase inhibition assay, and electron microscopy. Heavy meromyosin can overcome the effect of the brain protein and stimulate the polymerization of actin. The inhibition of ATPase activity is in part dependent upon the relative amounts of brain protein, actin, and myosin. The apparent molecular weight of the brain protein is approximately 20,000 daltons. It appears to be a heat‐labile glycoprotein containing 5{\textendash}6\% carbohydrate. 1983 International Society for Neurochemistry",

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TY - JOUR

T1 - Actin‐Stimulated Myosin Mg2+‐ATPase Inhibition by Brain Protein

AU - Berl, S.

AU - Chou, M.

AU - Mytilineou, C.

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N2 - Abstract: A low‐molecular‐weight protein, isolated from bovine brain, inhibits the actin‐stimulated Mg‐ATPase activity of myosin from striated muscle. This inhibition is probably related to its ability to cause actin to revert from its polymerized to its depolymerized state and to prevent the polymerization of actin. Its effect on the polymeric state of the actin has been demonstrated by viscosity studies, DNase inhibition assay, and electron microscopy. Heavy meromyosin can overcome the effect of the brain protein and stimulate the polymerization of actin. The inhibition of ATPase activity is in part dependent upon the relative amounts of brain protein, actin, and myosin. The apparent molecular weight of the brain protein is approximately 20,000 daltons. It appears to be a heat‐labile glycoprotein containing 5–6% carbohydrate. 1983 International Society for Neurochemistry

AB - Abstract: A low‐molecular‐weight protein, isolated from bovine brain, inhibits the actin‐stimulated Mg‐ATPase activity of myosin from striated muscle. This inhibition is probably related to its ability to cause actin to revert from its polymerized to its depolymerized state and to prevent the polymerization of actin. Its effect on the polymeric state of the actin has been demonstrated by viscosity studies, DNase inhibition assay, and electron microscopy. Heavy meromyosin can overcome the effect of the brain protein and stimulate the polymerization of actin. The inhibition of ATPase activity is in part dependent upon the relative amounts of brain protein, actin, and myosin. The apparent molecular weight of the brain protein is approximately 20,000 daltons. It appears to be a heat‐labile glycoprotein containing 5–6% carbohydrate. 1983 International Society for Neurochemistry

KW - Actin activation

KW - Brain inhibitory protein

KW - Myosin ATPase

UR - https://www.scopus.com/pages/publications/0020529828

U2 - 10.1111/j.1471-4159.1983.tb13582.x

DO - 10.1111/j.1471-4159.1983.tb13582.x

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AN - SCOPUS:0020529828

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